Evidence map›Paper›PMID 26690932›Full record

ArticleBMC plant biology2015

A small multigene hydroxyproline-O-galactosyltransferase family functions in arabinogalactan-protein glycosylation, growth and development in Arabidopsis.

Debarati Basu, Lu Tian, Wuda Wang, Shauni Bobbs, Hayley Herock, Andrew Travers, Allan M Showalter

Open access · goldAbstract read
In one paragraph

Article in BMC plant biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
6.7field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

52 citing papers in PubMed, 99 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Debarati BasuMolecular and Cellular Biology Program, Department of Environmental and Plant Biology, Ohio University, Athens, OH, 45701-2979, USA. db368709@ohio.edu.
Lu TianMolecular and Cellular Biology Program, Department of Environmental and Plant Biology, Ohio University, Athens, OH, 45701-2979, USA. lt140113@ohio.edu.
Wuda WangMolecular and Cellular Biology Program, Department of Environmental and Plant Biology, Ohio University, Athens, OH, 45701-2979, USA. ww805911@ohio.edu.
Shauni BobbsMolecular and Cellular Biology Program, Department of Environmental and Plant Biology, Ohio University, Athens, OH, 45701-2979, USA. sb355409@ohio.edu.
Hayley HerockMolecular and Cellular Biology Program, Department of Environmental and Plant Biology, Ohio University, Athens, OH, 45701-2979, USA. hh221509@ohio.edu.
Andrew TraversMolecular and Cellular Biology Program, Department of Environmental and Plant Biology, Ohio University, Athens, OH, 45701-2979, USA. at471413@ohio.edu.
Allan M ShowalterMolecular and Cellular Biology Program, Department of Environmental and Plant Biology, Ohio University, Athens, OH, 45701-2979, USA. showalte@ohio.edu.
Ohio University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundArabinogalactan-proteins (AGPs) are ubiquitous components of cell walls throughout the plant kingdom and are extensively post translationally modified by conversion of proline to hydroxyproline (Hyp) and by addition of arabinogalactan polysaccharides (AG) to Hyp residues. AGPs are implicated to function in various aspects of plant growth and development, but the functional contributions of AGP glycans remain to be elucidated. Hyp glycosylation is initiated by the action of a set of Hyp-O-galactosyltransferase (Hyp-O-GALT) enzymes that remain to be fully characterized.

resultsThree members of the GT31 family (GALT3-At3g06440, GALT4-At1g27120, and GALT6-At5g62620) were identified as Hyp-O-GALT genes by heterologous expression in tobacco leaf epidermal cells and examined along with two previously characterized Hyp-O-GALT genes, GALT2 and GALT5. Transcript profiling by real-time PCR of these five Hyp-O-GALTs revealed overlapping but distinct expression patterns. Transiently expressed GALT3, GALT4 and GALT6 fluorescent protein fusions were localized within Golgi vesicles. Biochemical analysis of knock-out mutants for the five Hyp-O-GALT genes revealed significant reductions in both AGP-specific Hyp-O-GALT activity and β-Gal-Yariv precipitable AGPs. Further phenotypic analysis of these mutants demonstrated reduced root hair growth, reduced seed coat mucilage, reduced seed set, and accelerated leaf senescence. The mutants also displayed several conditional phenotypes, including impaired root growth, and defective anisotropic growth of root tips under salt stress, as well as less sensitivity to the growth inhibitory effects of β-Gal-Yariv reagent in roots and pollen tubes.

conclusionsThis study provides evidence that all five Hyp-O-GALT genes encode enzymes that catalyze the initial steps of AGP galactosylation and that AGP glycans play essential roles in both vegetative and reproductive plant growth.

Indexed as

Gene Expression Regulation, PlantArabidopsisArabidopsis ProteinsGalactosyltransferasesGene Expression Regulation, DevelopmentalGlycosylationHydroxyprolineMucoproteinsMultigene FamilyNicotianaPlant ProteinsPlants, Genetically ModifiedArabidopsis Proteinsarabinogalactan proteinsGalactosyltransferasesHydroxyprolineMucoproteinsPlant Proteins

Identifiers

PMID26690932
PMCPMC4687291
OpenAlexW2211913568

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.